Lytic polysaccharide monooxygenases: enzymes for controlled and site-specific Fenton-like chemistry

B Bissaro, VGH Eijsink - Essays in biochemistry, 2023 - portlandpress.com
The discovery of oxidative cleavage of glycosidic bonds by enzymes currently known as lytic
polysaccharide monooxygenases (LPMOs) has profoundly changed our current …

How do metalloproteins tame the Fenton reaction and utilize• OH radicals in constructive manners?

B Wang, X Zhang, W Fang, C Rovira… - Accounts of Chemical …, 2022 - ACS Publications
Conspectus This Account describes the manner whereby nature controls the Fenton-type
reaction of O–O homolysis of hydrogen peroxide and harnesses it to carry out various useful …

Kβ X-ray Emission Spectroscopy of Cu(I)-Lytic Polysaccharide Monooxygenase: Direct Observation of the Frontier Molecular Orbital for H2O2 Activation

H Lim, MT Brueggemeyer, WJ Transue… - Journal of the …, 2023 - ACS Publications
Lytic polysaccharide monooxygenases (LPMOs) catalyze the degradation of recalcitrant
carbohydrate polysaccharide substrates. These enzymes are characterized by a …

Fenton-like Chemistry by a Copper(I) Complex and H2O2 Relevant to Enzyme Peroxygenase C–H Hydroxylation

B Kim, MT Brueggemeyer, WJ Transue… - Journal of the …, 2023 - ACS Publications
Lytic polysaccharide monooxygenases have received significant attention as catalytic
convertors of biomass to biofuel. Recent studies suggest that its peroxygenase activity (ie …

The “life-span” of lytic polysaccharide monooxygenases (LPMOs) correlates to the number of turnovers in the reductant peroxidase reaction

S Kuusk, VGH Eijsink, P Väljamäe - Journal of Biological Chemistry, 2023 - ASBMB
Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes that degrade the
insoluble crystalline polysaccharides cellulose and chitin. Besides the H 2 O 2 cosubstrate …

Histidine oxidation in lytic polysaccharide monooxygenase

M Torbjörnsson, MM Hagemann, U Ryde… - JBIC Journal of …, 2023 - Springer
The lytic polysaccharide monooxygenases (LPMOs) comprise a super-family of copper
enzymes that boost the depolymerisation of polysaccharides by oxidatively disrupting the …

[PDF][PDF] Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding

T Tandrup, SJ Muderspach, S Banerjee, G Santoni… - IUCrJ, 2022 - journals.iucr.org
The recently discovered lytic polysaccharide monooxygenases (LPMOs) are Cu-containing
enzymes capable of degrading polysaccharide substrates oxidatively. The generally …

Looking at LPMO reactions through the lens of the HRP/Amplex Red assay

AA Stepnov, VGH Eijsink - Methods in Enzymology, 2023 - Elsevier
Lytic polysaccharide monooxygenases (LPMOs) are unique redox enzymes capable of
disrupting the crystalline surfaces of industry-relevant recalcitrant polysaccharides, such as …

A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase

Y Liu, KA Harnden, C Van Stappen… - Proceedings of the …, 2023 - National Acad Sciences
The “Histidine-brace”(His-brace) copper-binding site, composed of Cu (His) 2 with a
backbone amine, is found in metalloproteins with diverse functions. A primary example is …

Protonation state of an important histidine from high resolution structures of lytic polysaccharide monooxygenases

S Banerjee, SJ Muderspach, T Tandrup, KEH Frandsen… - Biomolecules, 2022 - mdpi.com
Lytic Polysaccharide Monooxygenases (LPMOs) oxidatively cleave recalcitrant
polysaccharides. The mechanism involves (i) reduction of the Cu,(ii) polysaccharide …